Endoparasites observed within invertebrates used as live food items for captive wild birds: Overview and potential risks

To monitor and evaluate potential risks to birds’ health, invertebrate species that have been used as live food items had their body contents searched for endoparasites. The contents of approximately 10,000 invertebrates were analyzed. A principal component analysis was performed to study the relationship between the presence/absence of endoparasites and the characteristics of the invertebrates. In most of them, including the species preferred by birds such as caterpillars, waxworms, mealworms, most grasshoppers, and spiders, no organism was identified. Such findings suggest a low potential for parasite transmission associated with its consumption by birds. Although they had unknown or even unlikely implications for the birds’ health, gregarines, oxyurides Leidynema sp., and digenetic trematodes Monolecithotrema sp. were found in samples from woodlice, cockroaches, and centipedes, respectively. The only avian parasites observed in this study were Heterakis gallinarum in samples from earthworms and Acuaria spiralis from woodlice. Suggestively, soil invertebrates showed a higher prevalence of endoparasites and may represent a higher potential risk in comparison to the other categories of invertebrates sampled herein. Detritivory and collected origin were also explanatory variables related to the presence of endoparasites in the current study.     

Proteolytic analysis of domain structure in the beta heavy chain of dynein from sea urchin sperm flagella.

The stability of different regions of the beta heavy chain of dynein has been investigated by examining the perturbing effects of methanol, temperature, salt, and nucleotide on the pattern of tryptic digestion. In standard low-salt medium, tryptic proteolysis cleaves the beta heavy chain into three principal polypeptides of 130, 215, and 110 kDa, with the 215-kDa central peptide containing the ATP binding site as well as the vanadate and iron photocleavage sites (Mocz, G., Tang, W.-J. Y., & Gibbons, I. R. (1988) J. Cell Biol. 106, 1607-1614). The 130-kDa peptide is the most stable, and its susceptibility to trypsin appears unaffected by methanol concentrations up to 25% or temperatures up to 45 degrees C, although a 5-kDa region at one end is lost in the presence of salt (greater than 20 mM NaCl). The 215-kDa tryptic peptide contains two regions of different stability: its 123-kDa portion adjoining the 130-kDa peptide is destabilized by mild heat (37 degrees C) or by 25% methanol and becomes digested away to leave the more stable region of 92 kDa that is located toward the 110-kDa peptide and retains the V1 photocleavage site and most of the ATP binding site. The 110-kDa peptide is the least stable and at 37 degrees C, or in the presence of low concentrations of methanol or salt, it rapidly digested to small peptides. The presence of ATP during digestion of the beta heavy chain retards the formation of the 130- and 215-kDa peptides and also protects the 215-kDa peptide from further digestion at 37 degrees C.(ABSTRACT TRUNCATED AT 250 WORDS)     

Reproductive biology of the lane snapper,Lutjanus synagris (Linnaeus 1758) (Perciformes,Lutjanidae), in the Maranhão continental shelf,Northeast of Brazil

Environmental Biology of Fishes - To clarify the reproductive activity of lane snapper, Lutjanus synagris, a total of 359 specimens of lane snapper were collected in partnership with an artisanal...     

Effects of Ethanolic Extract of Cynara cardunculus (Artichoke) Leaves on Neuroinflammatory and Neurochemical Parameters in a Diet-Induced Mice Obesity Model

Neurochemical Research - This study aimed to evaluate the effect of Cynara cardunculus leaf ethanol extract on inflammatory and oxidative stress parameters in the hypothalamus, prefrontal cortex,...     

Electrophysiological characterization of Tityus obscurus β toxin 1 (To1) on Na+-channel isoforms

To1, previously named Tc49b, is a peptide neurotoxin isolated from venom of the scorpion Tityus obscurus that is responsible for lethal human poisoning cases in the Brazilian Amazonian region. Previously, To1 was shown to be lethal to mice and to change Na⁺ permeation in cerebellum granular neurons from rat brain. In addition, To1 did not affect Shaker B K⁺ channels. Based on sequence similarities, To1 was described as a β-toxin. In the present work, To1 was purified from T. obscurus venom and submitted to an electrophysiological characterization in human and invertebrate Na_V channels. The analysis of the electrophysiological experiments reveal that To1 enhances the open probability at more negative potentials of human Na_V 1.3 and 1.6, of the insect channel BgNa_V1 and of arachnid VdNa_V1 channel. In addition, To1 reduces the peak of Na⁺ currents in some of the Na_Vs tested. These results support the classification of the To1 as a β-toxin. A structure and functional comparison to other β-toxins that share sequence similarity to To1 is also presented.